Monoclonal antibodies development

Table 2 Cross-reactivity of racemic ractopamine and ractopamine glucuronide metabolites to a monoclonal antibody developed against racemic ractopamine...

De Guise, S. et al., Phenotyping of beluga whale blood lymphocytes using monoclonal antibodies, Develop. Comp. Immunol., 21, 425, 1997. 

Omalizumab and adalimumab are examples of monoclonal antibodies, developed for chronic non-life-threatening indication, that showed cross-reactivity to cynomolgus macaques as well as to humans. This broader species cross-reactivity allowed for a more thorough preclinical safety evaluation of the human monoclonal antibody developed for human use in the cynomolgus macaque. In the case of omalizumab, fertility studies and developmental tox-icitiy studies were conducted in macaques in addition to the chronic toxicity studies. For adalimumab, no reproductive and developmental toxicity studies were conducted. The value of conducting fertility and developmental studies in macaques with monoclonal antibodies is described in Chapter 17. 

Monoclonal antibodies developed by Kohler and Milstein25 imply the selection of the right B lymphocyte responsible for the secretion of the selected antibody and its fusion with a myeloma cell to assure longevity of secretion. 

The affinity matrices are often quite cosdy since they employ biochemicals such as lectins and monoclonal antibodies. Development of less expensive technology for production of fusion proteins may be am economical alternative. 

B72.3 is a monoclonal antibody developed from the membrane-enriched fraction of breast carcinoma in a patient with hver metastasis. The B72.3 reactive antigen was purified and called TAG-72 (tumor-associated glycoprotein). Further purification of TAG-72 from LS-174T human colon carcinoma xenograft produced a new generation of monoclonal antibodies with higher affinity. These antibodies, denoted cc for "colon carcinoma, were used in subsequent studies. 

CA 242 is a monoclonal antibody developed from a human colorectal carcinoma cell line, COLO 205. The antigenic... 

Shire, S. J. Gombotz, W. Bechtold-Peters, K. Andya, J., Eds. Current Trends in Monoclonal Antibody Development and Manufacturing, Springer New York New York (NY), 2010. 

Immunofluorescent detection of TS protein was done with the use of monoclonal antibodies, developed by in vivo immunization of Balb/c mice with homogeneous recombinant rat hepatoma TS protein as an antigen. The specific anti-rat TS antibodies recognized also T. spiralis TS, as indicated by cross-reactivity on Western blot. Localization of the enzyme was based on analysis of pictures collected by confocal microscopy. Two types of T spiralis muscle larvae preparations were studied muscle larvae isolated from mouse muscles by a procedure destroying nurse cells and muscle larvae remaining in nurse cells, isolated as an intact nurse cell preparation. 

Marc C, Clavel M-C, Rabie A (1986) Non-phosphorylated and phosphorylated neurofilaments in the cerebellum of the rat an immunocytochemical study using monoclonal antibodies. Development in normal and thyroid-deficient animals. Dev. Brain Res., 26, 249 260. 

Berry J D (2005). Rational monoclonal antibody development to emerging pathogens, biothreat agents and agents of foreign animal disease The antigen scale. Vet. J. 170 193-211. 

Omalizumab is a monoclonal antibody developed through somatic cell hybridization techniques and was identified as a murine anti-human IgE antibody, originally called MAE11 (48). It is designed to interact with the site that binds to FceRI on mast cells. Additional amino acid sequences have been incorporated into the antibody so that a humanized product resulted that only differs by 5% nonhuman amino acid residues. 

Recombinant antibodies offer a number of potential benefits over monoclonal antibodies, as they can be derived from almost any animal in which the immunoglobulin DNA sequences have been described. This aspect of recombinant antibody technology is of particular benefit, as biomarkers for disease diagnosis are often proteins and peptides, which are highly conserved in animals closely related to humans. This can be a particular problem in mice, which frequently develop tolerance for the immunizing antigen, rendering traditional monoclonal antibody development to... 

Hemoperfusion for acute poisoning—routine treatment in patients Hemoperfusion for aluminium and iron overload— routine treatment in patients Supplement to hemodialysis in end-stage renal failure—routine treatment in patients Artificial liver support hemoperfusion and hybrid systems—experimental Red blood cell substitutes for transfusion—Phase I and Phase 11 clinical trials Blood group antibodies removal (immunosorbents)—clinical trial Hereditary enzyme deficiency—clinical trial Clinical laboratory analysis—clinical application Production of monoclonal antibodies—development... 

Tanaka, H., Kinutani, M., Agata, A., Takashima, Y., and Obata, K. (1990) Pathfinding during spinal tract formation in quail-chick chimera analysed by species specific monoclonal antibodies. Development 110,565-571. 

Human monoclonal antibodies are made either by hybridomas from transgenic mice that have had their mouse antibody genes replaced with human antibody genes, or by a process called phage display. Human monoclonal antibodies end with the suffix -mumab. The first human monoclonal antibody developed through phage display technologies was adalimumab (Humira), which was approved by the FDA to treat several immune system diseases. 

Liu, J.K.H. (20122014) The history of monoclonal antibody development - Progress, remaining challenges and future innovations. Ann. Med. 

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